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Conserved domains on  [gi|17569739|ref|NP_510523|]
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RUN domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 9-161 2.08e-42

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


:

Pssm-ID: 439042  Cd Length: 145  Bit Score: 150.47  E-value: 2.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739   9 YRPQANYKRTQHGEFQNLVEGYVNkilretdiVDAENPNGRKLFNSIDTFFSYGLLTGDGTYWRCIRTFLPRAEQKMLIA 88
Cdd:cd17680   3 LRNISEAIKSLQSYSSSQEEEDVL--------ITNENRELQRLCEALDHALLHGLRRGNRGYWPFVKEFTHKETIKQIEN 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569739  89 ECGNANDRFLSVGWLKTSFNKGTLHFILLALNNQSNKayLTKFYHINACIRNSGLLEAITQFIEKLQPVQFAF 161
Cdd:cd17680  75 LPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKL--VKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 515-607 9.60e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 36.37  E-value: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739    515 TKSGFLFK---SNIGNWIKssdeaeqKYCMIVGNNFNVFADSTCK---TEELVISLSGSSINSTG-------RVAFQMKA 581
Cdd:smart00233   2 IKEGWLYKksgGGKKSWKK-------RYFVLFNSTLLYYKSKKDKksyKPKGSIDLSGCTVREAPdpdsskkPHCFEIKT 74

                           90       100
                   ....*....|....*....|....*..
gi 17569739    582 AEG-TFEFECPTQEDQIEWTRILTMIA 607
Cdd:smart00233  75 SDRkTLLLQAESEEEREKWVEALRKAI 101
 
Name Accession Description Interval E-value
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 9-161 2.08e-42

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 150.47  E-value: 2.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739   9 YRPQANYKRTQHGEFQNLVEGYVNkilretdiVDAENPNGRKLFNSIDTFFSYGLLTGDGTYWRCIRTFLPRAEQKMLIA 88
Cdd:cd17680   3 LRNISEAIKSLQSYSSSQEEEDVL--------ITNENRELQRLCEALDHALLHGLRRGNRGYWPFVKEFTHKETIKQIEN 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569739  89 ECGNANDRFLSVGWLKTSFNKGTLHFILLALNNQSNKayLTKFYHINACIRNSGLLEAITQFIEKLQPVQFAF 161
Cdd:cd17680  75 LPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKL--VKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 515-607 9.60e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 36.37  E-value: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739    515 TKSGFLFK---SNIGNWIKssdeaeqKYCMIVGNNFNVFADSTCK---TEELVISLSGSSINSTG-------RVAFQMKA 581
Cdd:smart00233   2 IKEGWLYKksgGGKKSWKK-------RYFVLFNSTLLYYKSKKDKksyKPKGSIDLSGCTVREAPdpdsskkPHCFEIKT 74

                           90       100
                   ....*....|....*....|....*..
gi 17569739    582 AEG-TFEFECPTQEDQIEWTRILTMIA 607
Cdd:smart00233  75 SDRkTLLLQAESEEEREKWVEALRKAI 101
 
Name Accession Description Interval E-value
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 9-161 2.08e-42

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 150.47  E-value: 2.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739   9 YRPQANYKRTQHGEFQNLVEGYVNkilretdiVDAENPNGRKLFNSIDTFFSYGLLTGDGTYWRCIRTFLPRAEQKMLIA 88
Cdd:cd17680   3 LRNISEAIKSLQSYSSSQEEEDVL--------ITNENRELQRLCEALDHALLHGLRRGNRGYWPFVKEFTHKETIKQIEN 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569739  89 ECGNANDRFLSVGWLKTSFNKGTLHFILLALNNQSNKayLTKFYHINACIRNSGLLEAITQFIEKLQPVQFAF 161
Cdd:cd17680  75 LPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKL--VKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 22-161 2.50e-06

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 47.80  E-value: 2.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739  22 EFQNLVEGYVNKILRETDIVDAENPNGRKLFNSIDTFFSYGL-----LTGDGTYWRCIRTFLPRAEQ-------KMLIAE 89
Cdd:cd17671   5 ELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLkpkrfGGGKVSFWDFLEALEKLLPApslkqaiRDINSL 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569739  90 CGNANDRFLSVGWLKTSFNKGTLHFILLALnnQSNKAYLTKFYHINACIRNSGLLEAITQFIEKLQPVQFAF 161
Cdd:cd17671  85 SNVKTDDGRGRAWIRLALNEKSLESYLAAL--LSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 515-607 9.60e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 36.37  E-value: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569739    515 TKSGFLFK---SNIGNWIKssdeaeqKYCMIVGNNFNVFADSTCK---TEELVISLSGSSINSTG-------RVAFQMKA 581
Cdd:smart00233   2 IKEGWLYKksgGGKKSWKK-------RYFVLFNSTLLYYKSKKDKksyKPKGSIDLSGCTVREAPdpdsskkPHCFEIKT 74

                           90       100
                   ....*....|....*....|....*..
gi 17569739    582 AEG-TFEFECPTQEDQIEWTRILTMIA 607
Cdd:smart00233  75 SDRkTLLLQAESEEEREKWVEALRKAI 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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